Cytosol aminopeptidase (P68767)

Identification
Name:Cytosol aminopeptidase
Synonyms:
  • Aminopeptidase A/I
  • Leucine aminopeptidase
  • LAP
  • Leucyl aminopeptidase
Gene Name:pepA
Enzyme Class:
Biological Properties
General Function:Involved in aminopeptidase activity
Specific Function:Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Required for plasmid ColE1 site-specific recombination but not in its aminopeptidase activity. Could act as a structural component of the putative nucleoprotein complex in which the Xer recombination reaction takes place
Cellular Location:Cytoplasmic
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Cysteinylglycine + 1.0Water → 1.0L-Cysteine + 1.0Glycine
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Cysteinylglycine + 1.0Water ↔ 1.0L-Cysteine + 1.0Glycine
ReactionCard
1.0R-S-Cysteinylglycine+1.0Thumb ↔ 1.0S-Substituted L-cysteine+1.0Thumb
1.0R-S-Cysteinylglycine + 1.0Water ↔ 1.0S-Substituted L-cysteine + 1.0Glycine
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Cysteinylglycine + 1.0Water → 1.0L-Cysteine + 1.0Glycine
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Water + 1.0L-Prolinylglycine → 1.0Glycine + 1.0L-Proline
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00078CysteinylglycineMetaboCard
ECMDB00123GlycineMetaboCard
ECMDB00574L-CysteineMetaboCard
ECMDB00162L-ProlineMetaboCard
ECMDB21237L-ProlinylglycineMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular
intracellular part
Function
aminopeptidase activity
binding
catalytic activity
cation binding
exopeptidase activity
hydrolase activity
ion binding
manganese ion binding
metal ion binding
metalloexopeptidase activity
metallopeptidase activity
peptidase activity
peptidase activity, acting on L-amino acid peptides
transition metal ion binding
Process
macromolecule metabolic process
metabolic process
protein metabolic process
proteolysis
Gene Properties
Blattner:b4260
Gene OrientationCounterclockwise
Centisome Percentage:96.61
Left Sequence End4482463
Right Sequence End4483974
Gene Sequence:
>1512 bp
ATGGAGTTTAGTGTAAAAAGCGGTAGCCCGGAGAAACAGCGGAGTGCCTGCATCGTCGTG
GGCGTCTTCGAACCACGTCGCCTTTCTCCGATTGCAGAACAGCTCGATAAAATCAGCGAT
GGGTACATCAGCGCCCTGCTACGTCGGGGCGAACTGGAAGGAAAACCGGGGCAGACATTG
TTGCTGCACCATGTTCCGAATGTACTTTCCGAGCGAATTCTCCTTATTGGTTGCGGCAAA
GAACGTGAGCTGGATGAGCGTCAGTACAAGCAGGTTATTCAGAAAACCATTAATACGCTG
AATGATACTGGCTCAATGGAAGCGGTCTGCTTTCTGACTGAGCTGCACGTTAAAGGCCGT
AACAACTACTGGAAAGTGCGTCAGGCTGTCGAGACGGCAAAAGAGACGCTCTACAGTTTC
GATCAGCTGAAAACGAACAAGAGCGAACCGCGTCGTCCGCTGCGTAAGATGGTGTTCAAC
GTGCCGACCCGCCGTGAACTGACCAGCGGTGAGCGCGCGATCCAGCACGGTCTGGCGATT
GCCGCCGGGATTAAAGCAGCAAAAGATCTCGGCAATATGCCGCCGAATATCTGTAACGCC
GCTTACCTCGCTTCACAAGCGCGCCAGCTGGCTGACAGCTACAGCAAGAATGTCATCACC
CGCGTTATCGGCGAACAGCAGATGAAAGAGCTGGGGATGCATTCCTATCTGGCGGTCGGT
CAGGGTTCGCAAAACGAATCGCTGATGTCGGTGATTGAGTACAAAGGCAACGCGTCGGAA
GATGCACGCCCAATCGTGCTGGTGGGTAAAGGTTTAACCTTCGACTCCGGCGGTATCTCG
ATCAAGCCTTCAGAAGGCATGGATGAGATGAAGTACGATATGTGCGGTGCGGCAGCGGTT
TACGGCGTGATGCGGATGGTCGCGGAGCTACAACTGCCGATTAACGTTATCGGCGTGTTG
GCAGGCTGCGAAAACATGCCTGGCGGACGAGCCTATCGTCCGGGCGATGTGTTAACCACC
ATGTCCGGTCAAACCGTTGAAGTGCTGAACACCGACGCTGAAGGCCGCCTGGTACTGTGC
GACGTGTTAACTTACGTTGAGCGTTTTGAGCCGGAAGCGGTGATTGACGTGGCGACGCTG
ACCGGTGCCTGCGTGATCGCGCTGGGTCATCATATTACTGGTCTGATGGCGAACCATAAT
CCGCTGGCCCATGAACTGATTGCCGCGTCTGAACAATCCGGTGACCGCGCATGGCGCTTA
CCGCTGGGTGACGAGTATCAGGAACAACTGGAGTCCAATTTTGCCGATATGGCGAACATT
GGCGGTCGTCCTGGTGGGGCGATTACCGCAGGTTGCTTCCTGTCACGCTTTACCCGTAAG
TACAACTGGGCGCACCTGGATATCGCCGGTACCGCCTGGCGTTCTGGTAAAGCAAAAGGC
GCCACCGGTCGTCCGGTAGCGTTGCTGGCACAGTTCCTGTTAAACCGCGCTGGGTTTAAC
GGCGAAGAGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:503
Protein Molecular Weight:54879
Protein Theoretical pI:7
PDB File:1GYT
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Cytosol aminopeptidase
MEFSVKSGSPEKQRSACIVVGVFEPRRLSPIAEQLDKISDGYISALLRRGELEGKPGQTL
LLHHVPNVLSERILLIGCGKERELDERQYKQVIQKTINTLNDTGSMEAVCFLTELHVKGR
NNYWKVRQAVETAKETLYSFDQLKTNKSEPRRPLRKMVFNVPTRRELTSGERAIQHGLAI
AAGIKAAKDLGNMPPNICNAAYLASQARQLADSYSKNVITRVIGEQQMKELGMHSYLAVG
QGSQNESLMSVIEYKGNASEDARPIVLVGKGLTFDSGGISIKPSEGMDEMKYDMCGAAAV
YGVMRMVAELQLPINVIGVLAGCENMPGGRAYRPGDVLTTMSGQTVEVLNTDAEGRLVLC
DVLTYVERFEPEAVIDVATLTGACVIALGHHITGLMANHNPLAHELIAASEQSGDRAWRL
PLGDEYQEQLESNFADMANIGGRPGGAITAGCFLSRFTRKYNWAHLDIAGTAWRSGKAKG
ATGRPVALLAQFLLNRAGFNGEE
References
External Links:
ResourceLink
Uniprot ID:P68767
Uniprot Name:AMPA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85677007
PDB ID:1GYT
Ecogene ID:EG10694
Ecocyc:EG10694
ColiBase:b4260
Kegg Gene:b4260
EchoBASE ID:EB0688
CCDB:AMPA_ECOLI
BacMap:16132082
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L., Blattner, F. R. (1995). "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Nucleic Acids Res 23:2105-2119. Pubmed: 7610040
  • Charlier, D., Hassanzadeh, G., Kholti, A., Gigot, D., Pierard, A., Glansdorff, N. (1995). "carP, involved in pyrimidine regulation of the Escherichia coli carbamoylphosphate synthetase operon encodes a sequence-specific DNA-binding protein identical to XerB and PepA, also required for resolution of ColEI multimers." J Mol Biol 250:392-406. Pubmed: 7616564
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • McCulloch, R., Burke, M. E., Sherratt, D. J. (1994). "Peptidase activity of Escherichia coli aminopeptidase A is not required for its role in Xer site-specific recombination." Mol Microbiol 12:241-251. Pubmed: 8057849
  • Stirling, C. J., Colloms, S. D., Collins, J. F., Szatmari, G., Sherratt, D. J. (1989). "xerB, an Escherichia coli gene required for plasmid ColE1 site-specific recombination, is identical to pepA, encoding aminopeptidase A, a protein with substantial similarity to bovine lens leucine aminopeptidase." EMBO J 8:1623-1627. Pubmed: 2670557
  • Strater, N., Sherratt, D. J., Colloms, S. D. (1999). "X-ray structure of aminopeptidase A from Escherichia coli and a model for the nucleoprotein complex in Xer site-specific recombination." EMBO J 18:4513-4522. Pubmed: 10449417